IP Library › Granted Patent US 12,268,727
Granted Patent B2
US 12,268,727 · App. 17/350,746 · Granted Apr 8, 2025

Bioactive polypeptides for improvements in plant protection, growth and productivity

Inventors: Brian Thompson (Creve Coeur, MO); Michelle Leslie (Webster Groves, MO)
Assignee: Spogen Biotech Inc.
A61K38/16A01N37/46A01N63/10A01N63/50C07K14/195C07K14/21C07K14/245C07K14/27C07K14/32C12N1/20C12N15/82C12P21/02A01N63/22A01N63/25C12N2510/02
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Quick Facts
Patent No.
US 12,268,727
App. No.
17/350,746
Granted
Apr 8, 2025
Kind
B2
Abstract

Bioactive priming polypeptides are provided that are useful when applied to plants in agricultural formulations. Methods of using the formulations containing the bioactive priming polypeptides are also provided which are applied exogenously to the surface of a plant or a plant cell membrane or endogenously to the interior of a plant or to a plant cell. The bioactive priming polypeptides when applied to a plant, a plant part, or a plant growth medium or a rhizosphere in an area surrounding the plant or the plant part increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture.

Claims (55)

1. An isolated flagellin or flagellin-associated peptide for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, wherein:

the peptide consists of the amino acid sequence SEQ ID NO: 752; and

a) arginine at amino acid position 1 of SEQ ID NO: 752 is optionally substituted with glutamine or lysine; or

b) serine at amino acid position 4 of SEQ ID NO: 752 is optionally substituted with glycine, threonine, asparagine, or arginine; or

c) lysine at amino acid position 6 of SEQ ID NO: 752 is optionally substituted with serine, alanine or glycine; or

d) aspartic acid at amino acid position 8 of SEQ ID NO: 752 is optionally substituted with proline; or

e) alanine at amino acid position 9 of SEQ ID NO: 752 is optionally substituted with proline; or

f) the flagellin or flagellin-associated peptide optionally has a chemical modification selected from the group consisting of acetylation, amidation, cyclization, and PEGylation, is part of a fusion protein wherein the fusion protein contains a protease recognition sequence, or a combination thereof; or

g) the peptide is optionally part of a fusion protein and the fusion protein has a signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or a signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or a combination thereof; or a secretion peptide, wherein the amino acid sequence of the secretion peptide has any one of SEQ ID NOs: 563-570 or 769.

2. The isolated peptide of claim 1 , wherein the flagellin or flagellin-associated peptide has a substitution selected from the group consisting of:

a) arginine at amino acid position 1 of SEQ ID NO: 752 is substituted with glutamine or lysine;

b) serine at amino acid position 4 of SEQ ID NO: 752 is substituted with glycine, threonine, asparagine, or arginine;

c) lysine at amino acid position 6 of SEQ ID NO: 752 is substituted with serine, alanine or glycine;

d) aspartic acid at amino acid position 8 of SEQ ID NO: 752 is substituted with proline; and

e) alanine at amino acid position 9 of SEQ ID NO: 752 is substituted with proline.

3. The peptide of claim 2 , wherein the flagellin or flagellin-associated peptide: has the chemical modification, is part of the fusion protein wherein the fusion protein-contains the protease recognition sequence, or the combination thereof.

4. The peptide of claim 3 , wherein the flagellin or flagellin-associated peptide has the chemical modification.

5. The peptide of claim 2 , wherein the peptide is part of the fusion protein and the fusion protein the secretion peptide, wherein the amino acid sequence of the secretion peptide has any one of SEQ ID NOS: 563-570 or 769.

6. The peptide of claim 2 , wherein the peptide is chemically synthesized, concentrated from a fermentation product, and/or purified, by filtration, chromatography, or from a recombinant microorganism.

7. A composition for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, the composition comprising the peptide of claim 2 and an agrochemical or a carrier.

8. A seed coated with the peptide of claim 2 , a composition comprising the peptide and a carrier or agrochemical, or a recombinant microorganism expressing or overexpressing at least the peptide.

9. The peptide of claim 1 , wherein the flagellin or flagellin-associated peptide: has the chemical modification, is part of the fusion protein wherein the fusion protein-contains the protease recognition sequence, or the combination thereof.

10. The peptide of claim 9 , wherein the flagellin or flagellin-associated peptide has the chemical modification.

11. The peptide of claim 1 , wherein the peptide is part of the fusion protein and the fusion protein the secretion peptide, wherein the amino acid sequence of the secretion peptide has any one of SEQ ID NOS: 563-570 or 769.

12. The peptide of claim 11 , wherein the peptide is part of the fusion protein and the fusion protein has the signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or the peptide is part of the fusion protein and the fusion protein has the signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or combination thereof.

13. The peptide of claim 1 , wherein the peptide is chemically synthesized, concentrated from a fermentation product, and/or purified, by filtration, chromatography, or from a recombinant microorganism.

14. A composition for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, the composition comprising the peptide of claim 1 and an agrochemical or a carrier.

15. A seed coated with the peptide of claim 1 , a composition comprising the peptide and a carrier or agrochemical, or a recombinant microorganism expressing or overexpressing at least the peptide.

16. An isolated flagellin or flagellin-associated peptide for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, wherein:

the peptide consists of the amino acid sequence SEQ ID NO: 753 ; and

a) aspartic acid at amino acid position 1 of the 22 amino acid peptide is optionally substituted with aspartic acid, asparagine, glutamic acid, glycine, glutamine, leucine or threonine; or

b) arginine at amino acid position 2 of the 22 amino acid peptide is optionally substituted with lysine; or

c) leucine at amino acid position 3 of the 22 amino acid peptide is optionally substituted with isoleucine; or

d) lysine at amino acid position 7 of the 22 amino acid peptide is optionally substituted with leucine, glutamine, tyrosine or serine; or

e) arginine at amino acid position 8 of the 22 amino acid peptide is optionally substituted with glutamine or lysine; or

f) serine at amino acid position 11 of the 22 amino acid peptide is optionally substituted with glycine, threonine, asparagine, or arginine; or

g) serine at amino acid position 13 of the 22 amino acid peptide is optionally substituted with lysine, alanine or glycine; or

h) alanine at amino acid position 16 of the 22 amino acid peptide is optionally substituted with proline; or

i) leucine at amino acid position 19 of the 22 amino acid peptide is optionally substituted with glutamine; or

j) alanine at amino acid position 20 of the 22 amino acid peptide is optionally substituted with glutamine; or

k) alanine at amino acid position 22 of the 22 amino acid peptide is optionally substituted with serine; or

l) the flagellin or flagellin-associated peptide optionally has a chemical modification selected from the group consisting of acetylation, amidation, cyclization, and PEGylation, is part of a fusion protein wherein the fusion protein-contains a protease recognition sequence, or a combination thereof; or

m) the peptide is optionally part of a fusion protein and the fusion protein has a signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or a signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or a combination thereof; or a secretion peptide, wherein the amino acid sequence of the secretion peptide has any one of SEQ ID NOs: 563-570 or 769.

17. The peptide of claim 16 , wherein the peptide is part of the fusion protein and the fusion protein has the signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or the peptide is part of the fusion protein and the fusion protein has the signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or a combination thereof.

18. The peptide of claim 16 , wherein the peptide is chemically synthesized, concentrated from a fermentation product, and/or purified, by filtration, chromatography, or from a recombinant microorganism.

19. A composition for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, the composition comprising the peptide of claim 16 and an agrochemical or a carrier.

20. A seed coated with the peptide of claim 16 , a composition comprising the peptide and a carrier or agrochemical, or a recombinant microorganism expressing or overexpressing at least the peptide.

21. An isolated flagellin or flagellin-associated peptide for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, wherein:

the peptide consists of the amino acid sequence of any one of SEQ ID NOs: 754, 756, 758, 761, and 763-765; and

a) the flagellin or flagellin-associated peptide optionally has a chemical modification selected from the group consisting of acetylation, amidation, cyclization, and PEGylation, is part of a fusion protein wherein the fusion protein-contains a protease recognition sequence, or a combination thereof; or

b) the peptide is optionally part of a fusion protein and the fusion protein has a signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or a signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or a combination thereof; or a secretion peptide, wherein the amino acid sequence of the secretion peptide has any one of SEQ ID NOs: 563-570 or 769.

22. The peptide of claim 21 , wherein the peptide is part of the fusion protein and the fusion protein has the signature peptide, wherein the amino acid sequence of the signature peptide has any one of SEQ ID NOs: 542-548, or any combination thereof; or the peptide is part of the fusion protein and the fusion protein has the signal anchor sorting peptide, wherein the amino acid sequence of the signal anchor sorting peptide has any one of SEQ ID NOs: 549-562, or a combination thereof.

23. The peptide of claim 21 , wherein the peptide is chemically synthesized, concentrated from a fermentation product, and/or purified, by filtration, chromatography, or from a recombinant microorganism.

24. A composition for bioactive priming of a plant or a plant part to increase growth, yield, health, longevity, productivity, and/or vigor of a plant or a plant part and/or decrease abiotic stress in the plant or the plant part and/or protect the plant or the plant part from disease, insects and/or nematodes, and/or increase the innate immune response of the plant or the plant part and/or change plant architecture, the composition comprising the peptide of claim 21 and an agrochemical or a carrier.

25. A seed coated with the peptide of claim 21 , a composition comprising the peptide and a carrier or agrochemical, or a recombinant microorganism expressing or overexpressing at least the peptide.

Assignments (3)
SECURITY INTEREST Recorded Jan 23, 2023
From: SPOGEN BIOTECH INC; ELEMENTAL ENZYMES AG AND TURF, LLC; THOMPSON, BRIAN M; THOMPSON, KATIE C
To: GENISYS CREDIT UNION
Reel/Frame 062458/0476 →
SECURITY INTEREST Recorded Jan 23, 2023
From: SPOGEN BIOTECH INC; ELEMENTAL ENZYMES AG AND TURF, LLC; THOMPSON, BRIAN M; THOMPSON, KATIE C
To: GENISYS CREDIT UNION
Reel/Frame 062458/0544 →
ASSIGNMENT OF ASSIGNOR'S INTEREST Recorded Sep 14, 2021
From: THOMPSON, BRIAN; LESLIE, MICHELLE
To: SPOGEN BIOTECH INC.
Reel/Frame 057475/0337 →
Continuity (4)
Division 16929422 · Jul 15, 2020
Division 16041059 · Jul 20, 2018
Provisional Application 62534710 · Jul 20, 2017
Related Publication 20230016543A1 · Jan 19, 2023
References Cited (178)
US 5631007A · Ryals et al. · 1997 [cited by applicant]
US 5668007A · Spencer et al. · 1997 [cited by applicant]
US 5851953A · Pehu et al. · 1998 [cited by applicant]
US 5922649A · Pehu et al. · 1999 [cited by applicant]
US 5952267A · Mottram · 1999 [cited by applicant]
US 5972840A · Mottram · 1999 [cited by applicant]
US 6083876A · Jokinen et al. · 2000 [cited by applicant]
US 6281411B1 · Adams et al. · 2001 [cited by applicant]
US 6413908B1 · Reekmans et al. · 2002 [cited by applicant]
US 6460290B1 · Moore et al. · 2002 [cited by applicant]
US 6593275B1 · Unkefer et al. · 2003 [cited by applicant]
US 6831040B1 · Unkefer et al. · 2004 [cited by applicant]
US 6927322B2 · Stewart et al. · 2005 [cited by applicant]
US 7410800B2 · Bensen et al. · 2008 [cited by applicant]
US 7517684B2 · Rubenfield et al. · 2009 [cited by applicant]
US 7914802B2 · Rhee et al. · 2011 [cited by applicant]
US 7915381B2 · Anderem et al. · 2011 [cited by applicant]
US 8007812B2 · Gudkov · 2011 [cited by examiner]
US 8263078B2 · Rachamim et al. · 2012 [cited by applicant]
US 8618059B2 · Gudkov et al. · 2013 [cited by applicant]
US 8703146B2 · Aderem et al. · 2014 [cited by applicant]
US 8883174B2 · Dickey et al. · 2014 [cited by applicant]
US 9006180B2 · Gudkov et al. · 2015 [cited by applicant]
US 9061002B2 · Gomez Casado · 2015 [cited by applicant]
US 9085616B2 · Aderem et al. · 2015 [cited by applicant]
US 9101144B2 · Doktycz et al. · 2015 [cited by applicant]
US 9186400B2 · Dickey et al. · 2015 [cited by applicant]
US 9205095B2 · Gudkov · 2015 [cited by applicant]
US 9222103B2 · Zipfel et al. · 2015 [cited by applicant]
US 9314484B2 · Blander et al. · 2016 [cited by applicant]
US 9457061B2 · Gudkov et al. · 2016 [cited by applicant]
US 9463230B2 · Emery et al. · 2016 [cited by applicant]
US 9499823B2 · De Lorenzo et al. · 2016 [cited by applicant]
US 10034926B2 · Gleiberman et al. · 2018 [cited by applicant]
US 10306895B2 · Chen et al. · 2019 [cited by applicant]
US 10336793B2 · Gudkov et al. · 2019 [cited by applicant]
US 10717767B2 · Thompson et al. · 2020 [cited by applicant]
US 11046735B2 · Thompson et al. · 2021 [cited by applicant]
US 20030044429A1 · Aderem et al. · 2003 [cited by applicant]
US 20070065902A1 · Dicosimo et al. · 2007 [cited by applicant]
US 20070128183A1 · Meinke et al. · 2007 [cited by applicant]
US 20080120740A1 · Frank et al. · 2008 [cited by applicant]
US 20090297552A1 · Aderem et al. · 2009 [cited by applicant]
US 20100015170A1 · Takeshita et al. · 2010 [cited by applicant]
US 20100239583A1 · Murthy et al. · 2010 [cited by applicant]
US 20100285532A1 · Berger et al. · 2010 [cited by applicant]
US 20110008383A1 · Powell et al. · 2011 [cited by applicant]
US 20120082700A1 · Dickey et al. · 2012 [cited by applicant]
US 20120137392A1 · De Lorenzo et al. · 2012 [cited by applicant]
US 20120151636A1 · Ronald et al. · 2012 [cited by applicant]
US 20130108661A1 · Blander et al. · 2013 [cited by applicant]
US 20130324462A1 · Gudkov et al. · 2013 [cited by applicant]
US 20130331548A1 · Nakaar et al. · 2013 [cited by applicant]
US 20140255441A1 · Compans et al. · 2014 [cited by applicant]
US 20140274707A1 · Thompson et al. · 2014 [cited by applicant]
US 20140295012A1 · Kutsch et al. · 2014 [cited by applicant]
US 20150064219A1 · Blander et al. · 2015 [cited by applicant]
US 20150110827A1 · Song et al. · 2015 [cited by applicant]
US 20150125492A1 · Dickey et al. · 2015 [cited by applicant]
US 20150165009A1 · Gewirtz et al. · 2015 [cited by applicant]
US 20150182587A1 · Gudkov et al. · 2015 [cited by applicant]
US 20150191742A1 · Zimmerli et al. · 2015 [cited by applicant]
US 20150216926A1 · Kutsch · 2015 [cited by applicant]
US 20160022767A1 · Neish et al. · 2016 [cited by applicant]
US 20160031948A1 · Thompson et al. · 2016 [cited by applicant]
US 20160073640A1 · Curtis et al. · 2016 [cited by applicant]
US 20160074508A1 · Dickey et al. · 2016 [cited by applicant]
US 20160108096A1 · Thompson et al. · 2016 [cited by applicant]
US 20160165890A1 · Matsuzaki · 2016 [cited by applicant]
US 20160166671A1 · Tussey et al. · 2016 [cited by applicant]
US 20160193319A1 · Mizel et al. · 2016 [cited by applicant]
US 20160193329A1 · Song et al. · 2016 [cited by applicant]
US 20160206690A1 · Gleiberman et al. · 2016 [cited by applicant]
US 20160220660A1 · Song et al. · 2016 [cited by applicant]
US 20160302416A1 · Fefer et al. · 2016 [cited by applicant]
US 20170292108A1 · Wei · 2017 [cited by applicant]
US 20170332645A1 · Chen et al. · 2017 [cited by applicant]
US 20180099999A1 · Thompson et al. · 2018 [cited by applicant]
US 20180325103A1 · Thompson · 2018 [cited by applicant]
CN 105950312A · 2016 [cited by applicant]
CN 107208072A · 2017 [cited by applicant]
EA 23386B1 · 2016 [cited by applicant]
RU 2444880C2 · 2012 [cited by applicant]
RU 2563930C1 · 2015 [cited by applicant]
WO 9607319A1 · 1996 [cited by applicant]
WO 9826081A1 · 1998 [cited by applicant]
WO 9949047A2 · 1999 [cited by applicant]
WO 20000066740A · 2000 [cited by applicant]
WO 2002072782A2 · 2002 [cited by applicant]
WO 2005070455A1 · 2005 [cited by applicant]
WO 2006069198A1 · 2006 [cited by applicant]
WO 2006097482A1 · 2006 [cited by applicant]
WO 2009102818A1 · 2009 [cited by applicant]
WO 2010111485A1 · 2010 [cited by applicant]
WO 2010117978A1 · 2010 [cited by applicant]
WO 2011097573A2 · 2011 [cited by applicant]
WO 2011146612A2 · 2011 [cited by applicant]
WO 2012097012A1 · 2012 [cited by applicant]
WO 2013144579A1 · 2013 [cited by applicant]
WO 2016007606A2 · 2016 [cited by applicant]
WO 2016011179A2 · 2016 [cited by applicant]
WO 2016044542A1 · 2016 [cited by applicant]
WO 2016044768A1 · 2016 [cited by applicant]
WO 2016044661A1 · 2016 [cited by applicant]
WO WO2016039961A1 · 2016 [cited by examiner]
WO 2017001927A1 · 2017 [cited by applicant]
WO 2017161091A1 · 2017 [cited by applicant]
WO 2019018768A1 · 2019 [cited by applicant]
Penn State Extension, Agricultural Alternatives, Pepper Production, extension.psu.edu, 2010, 6 pages. [cited by applicant]
Penn State Extension, Agricultural, Tomato Production, extension.psu.edu, 2016, 8 pages. [cited by applicant]
Corn Growth and Management Quick Guide, North Dakota State University, www.ag.ndsu.edu, 2013, 8 pages. [cited by applicant]
Saline and Sodic Soils, North Dakota State University Extension Service, www.ag.ndsu.edu, Date Unknown, 8 pages. [cited by applicant]
Examination Report in AU2018304469, mailed Jun. 21, 2022, 6 pages. [cited by applicant]
Flg22 peptide (30-51 aa, Flic, [cited by applicant]
Garcia et al., “ [cited by applicant]
Accession WP_097951446, “flagellin [ [cited by applicant]
Gomez-Gomez, L., et al, “Flagellin perception: a paradigm for innate immunity,”Trends in Plant Science, 2002, pp. 251-256, vol. 7 No. 6. [cited by applicant]
Dill, G. M., “Glyphosate-resistant Crops: History, Status and Future,” Pest Management Science, 2005, pp. 219-224, vol. 61. [cited by applicant]
Duan, P., et al, “Naturally ocuring betaine grafted on cotton fabric for achieving antibacterial and anti-protein adsorption functions” Cellulose, 2020, pp. 6603-6615, vol. 27. [cited by applicant]
Fosternic, V., et al, “The role of the C-terminal D0 domain of flagellin in activation of Toll like receptor 5,” PLOS Pathogens, 2017, 20 pages. [cited by applicant]
Schulz, T., et al, “Soybean Seed Inoculent and Fungicidal Seed Treatment Effects on Soybean,” Crop Science, 2008, pp. 1975-1983, vol. 48. [cited by applicant]
Hao, G., et al, “Induction of innate immune responses by flagellin from the intracellular bacterium, ‘Candidatus Liberibacter solanacearum’,” BMC Plant Biology, 2014, pp. 1471-2229, vol. 14:211. [cited by applicant]
Felitsky, D., et al, “The Exclusion of Glycine Betaine from Anionic Biopolumer Surface Why Glycine Betaine Is am Effective Osmoprotectant but Also a Compatibke Solute”, Biochemistry, 2004, pp. 14732-14743, vol. 43. [cited by applicant]
Accession WP_064449846, “flagellin [ [cited by applicant]
Berger, Eldie, et al., “Extracellular secretion of a recombinant therapeutic peptide by Bacillus halodrans utilizing a modified flagellin type III secretion system”, Microbial Cell Factories, 2011, vol. 10, issue 62. [cited by applicant]
Meng, Qingfeng, et al., “A proteomic insight into the MSP1 and flg22 induced signaling in [cited by applicant]
Xu, Dong, et al., “Sequence Diversity of the Bacillus thuringiensis and B. cereus Sensu Lato Flagellin (H Antigen) Protein: Comparison with H Serotype Diversity” Applied and Environmental Microbiology, Jul. 2006, pp. 46… [cited by applicant]
European Patent Office, Partial European Search Report issued Dec. 12, 2022 Application No. 20745065.1. [cited by applicant]
Chinchilla, D., et al., “The [cited by applicant]
Choi, M.-S., et al., “Harpins, Multifunctional Proteins Secreted by Gram-Negative Plant-Pathogenic Bacteria,” Molecular Plant-Microbe Interactions, 2013, pp. 1115-1122, vol. 26, No. 10. [cited by applicant]
Engelhardt, S., et al., “Separable Roles of the [cited by applicant]
Felix, G., et al., “Plants Have A Sensitive Perception System for the Most Conserved Domain of Bacterial Flagellin,” The Plant Journal, 1999, pp. 265-276, vol. 18, No. 3. [cited by applicant]
Garcia, AV., et al. “ [cited by applicant]
Gohre, V., et al., “Molecular crosstalk between PAMP-triggered immunity and photosynthesis.” Molecular Plant-Microbe Interactions, 2012, pp. 1083-1092, vol. 8. [cited by applicant]
Gomez-Gomez, L., et al., “FLS2: An LRR Receptor-like Kinase Involved in the Perception of the Bacterial Elicitor Flagellin in [cited by applicant]
Gottwald, T. R., et al., “Citrus Canker,” The Plant Health Instructor, 2005, 10 pages. [cited by applicant]
Guptasarma, P., “Reversal of Peptide Backbone Direction May Result in the Mirroring of Protein Structure,” FEBS Letters, Oct. 1992, pp. 205-210, vol. 310, No. 3. [cited by applicant]
Halbert, S.E., et al., “Asian Citrus Psyllids ( [cited by applicant]
Hu, H., et al., “Quantification of Live ‘Candiatus Liberibacter asiaticus’ Populations Using Real-Time PCR and Propidium Monoazide,” Plant Disease, Sep. 2013, pp. 1158-1167, vol. 97, No. 9. [cited by applicant]
International Search Report and Written Opinion issued for PCT/US2018/043092 dated Nov. 15, 2018, 18 pages. [cited by applicant]
JBT FoodTech, “Procedures for Analysis of Citrus Products,” Laboratory Manual,, Sixth Edition, 2011, 193 pages. [cited by applicant]
Kim, J.-G., et al., “Mutational Analysis of Xanthomonas Harpin HpaG Identifies A Key Functional Region that Elicits the Hypersensitive Response in Nonhost Plants,” Journal of Bacteriology, Sep. 2004, pp. 6239-6247, vol.… [cited by applicant]
Kutschmar, A., et al., “PSK-alpha Promotes Root Growth in [cited by applicant]
Lorbiecke, R., et al., “Comparative Analysis of PSK Peptide Growth Factor Precursor Homologs,” Plant Science, 2002, pp. 321-332, vol. 163, No. 2. [cited by applicant]
Matsubayashi, Y., et al., “Phytosulfonkine-alpha, A sulfated Pentapeptide, Stimulates the Proliferation of Rice Cells by Means of Specific High- and Low-Affinity Binding Sites,” Proceedings of the National Academy of Sc… [cited by applicant]
Matsubayashi, Y., et al., “The Endogenous Sulfated Pentapeptide Phytosulfokine-alpha Stimulates Tracheary Element Differentiation of Isolated Mesophyll Cells of Zinnia,” Plant Physiology, Aug. 1999, pp. 1043-1048, vol. … [cited by applicant]
Matsumiya, Y., et al., “Soybean Peptide: Novel Plant Growth Promoting Peptide from Soybean,” Soybean and Nutrition, Chapter 11, Intech, 2011, pp. 215-230. [cited by applicant]
Meindl, T., et al., “The Bacterial Elicitor Flagellin Activates Its Receptor in Tomato Cells According to the Address-Message Concept,” The Plant Cell, Sep. 2000, pp. 1783-1794, vol. 12. [cited by applicant]
Nawrot, R., et al., “Plant Antimicrobial Peptides,” Folia Microbiologica, 2014, pp. 181-196, vol. 59, No. 3. [cited by applicant]
Pond, L., et al., “A Role of Acidic Residues in Di-leucine Motif-based Targeting to the Endocytic Pathway,” The Journal of Biological Chemistry, Aug. 1995, pp. 19989-19997, vol. 270, No. 34. [cited by applicant]
Ryan, C.A., et al., “Polypeptide Hormones,” The Plant Cell, 2002, pp. S251-S264, Supplement 2002. [cited by applicant]
Sauter, M., “Phytosulfokine Peptide Signalling,” Journal of Experimental Botany, 2015, pp. 5161-5169, vol. 66, No. 17. [cited by applicant]
Takai, R., et al., “Analysis of Flagellin Perception Mediated by flg22 Receptor OsFLS2 in Rice,” Molecular Plant-Microbe Interactions, 2008, pp. 1635-1642, vol. 21, No. 12. [cited by applicant]
Tam, J. P., et al., “Antimicrobial Peptides from Plants,” Pharmaceuticals, 2015, pp. 711-757, vol. 8, No. 4. [cited by applicant]
Yoshiki, M., et al., “Soybean as a Nitrogen Supplier,” Chapter 3, Intech, 2013, pp. 49-60. [cited by applicant]
Zhang, C., et al., “Harpin-Induced Expression and Transgenic Overexpression of the Phloem Protein Gene AtPP2-A1 in [cited by applicant]
Zhang, W., et al., “The plant innate immunity response in stomatal guard cells invokes G-protein-dependent ion channel regulation,” The Plant Journal, 2008, pp. 984-996, vol. 56. [cited by applicant]
Zeigler, D., et al., Bacillus Genetic Stock Center Catalog of Strains, Seventh Edition, Part 2: Bacillus thuringiensis and Bacillus cereus, 1999, 58 pages. [cited by applicant]
Zipfel, C., et al., “Bacterial Disease Resistance in [cited by applicant]
Zipfel, C., et al., “Perception of the Bacterial PAMP EFa-Tu by the Receptor EFS Restricts Agrobacterium-Mediated Transformation,” Cell, May 2006, pp. 749-760, vol. 125. [cited by applicant]
International Search Report and Written Opinion issued for PCT/US2020/014591 dated Jun. 1, 2020, 10 pages. [cited by applicant]
Aroca, A., et al., “S-Sulfhydration: A Cysteine Posttranslational Modification in Plant Systems,” Plant Physiology, 2015, pp. 334-342, vol. 168, No. 1. [cited by applicant]
Gottwald, T. R., “Current Epidemiological Understanding of Citrus Huanglongbing,” Annual Review of Phytopathology, 2010, pp. 119-139, vol. 48. [cited by applicant]
Jaffe, M. J., et al., “Callose Deposition During Gravitropism of [cited by applicant]
Keppler, B. D., et al., “3-Aminobenzamide Blocks MAMP-Induced Callose Deposition Independently of Its Poly (ADPribosyl)ation Inhibiting Activity,” Frontiers in Plant Science, 2018, pp. 1-13, vol. 9, Article 1907. [cited by applicant]
Koh, E. J., et al., “Callose Deposition in the Phloem Plasmodesmata and Inhibition of Phloem Transport in Citrus Leaves Infected with “Candidatus Liberibacter asiaticus”,” Protoplasma, 2012, pp. 687-697, vol. 249, No. 3. [cited by applicant]
El Sabagh, A., et al., “Alleviation of Adverse Effects of Salt Stress on Soybean ( [cited by applicant]
Mcneil, S. D., et al., “Betaines and Related Osmoprotectants. Targets for Metabolic Engineering of Stress Resistance,” Plant Physiology, Aug. 1999, pp. 945-949, vol. 120. [cited by applicant]
Moghaieb, R. E. A., et al., “Effect of Salinity on Osmotic Adjustment, Glycinebetaine Accumulation and the Betaine Aldehyde Dehydrogenase Gene Expression in Two Halophytic Plants, Salicornia europaea and Suaeda maritima… [cited by applicant]
Molazem, D., et al., Role of Proline, Na and Chlorophyll Content in Salt Tolerance of Corn ( [cited by applicant]
Molla, R., et al., “Exogenous Proline and Betaine-induced Upregulation of Glutathione Transferase and Glyoxalase I in Lentil ( [cited by applicant]
Naeve, S., “Soybean Production—Growth Stages,” [https://www.extension.umn.edu/agriculture/soybean/growth-and-development], Mar. 23, 2018, 3 pages. [cited by applicant]
Phillips, D. A., et al., “Trigonelline and Stachydrine Released from Alfalfa Seeds Activate NodD2 Protein in Rhizobium meliloti,” Plant Physiology, 1992, pp. 1526-1531, vol. 99, Number. [cited by applicant]
Rossi, A. M. et al., “Nitrogen Contents in Food: A Comparison Between the Kjeldahl and Hach Methods,” The Journal of the Argentine Chemical Society, 2004, pp. 99-108, vol. 92, Nos. 4/6. [cited by applicant]
Siddique, A. B., et al., “Mitigation of Salt Stress by Foliar Application of Proline in Rice,” Universal Journal of Agricultural Research, 2015, pp. 81-88, vol. 3, No. 3. [cited by applicant]
Slama, I., et al., “Diversity, Distribution and Roles of Osmoprotective Compounds Accumulated in Halophytes Under Abiotic Stress,” Annals of Botany, 2014, 15 pages. [cited by applicant]
Sobahan, M. A., et al., Exogenous Proline and Glycinebetaine Suppress Apoplastic Flow to Reduce Na+ Uptake in Rice Seedlings, Bioscience, Biotechnology, and Biochemistry, 2009, pp. 2037-2042, vol. 73, No. 9. [cited by applicant]
Zhang, L., et al., “Exogenous Glycinebetaine and Humic Acid Improve Growth, Nitrogen Status, Photosynthesis, and Antioxidant Defense System and Confer Tolerance to Nitrogen Stress in Maize Seedlings,” Journal of Plant I… [cited by applicant]